Rhodobacter sphaeroides haem protein: a novel cytochrome with nitric oxide dioxygenase activity

Bor-Ran Li, J L Ross Anderson, Christopher G Mowat, Caroline S Miles, Graeme A Reid, Stephen K Chapman

    Research output: Contribution to journalArticle

    Abstract

    Rhodobacter sphaeroides produces a novel cytochrome, designated as SHP (sphaeroides haem protein), that is unusual in having asparagine as a redox-labile haem ligand. The gene encoding SHP is contained within an operon that also encodes a DHC (dihaem cytochrome c) and a membrane-associated cytochrome b. DHC and SHP have been shown to have high affinity for each other at low ionic strength (K-d = 0.2 mu M), and DHC is able to reduce SHP very rapidly. The reduced form of the protein, SHp(2+) (reduced of ferrous SHP), has high affinity for both oxygen and nitric oxide (NO). it has been shown that the oxyferrous form, SHp(2+) -O-2 (oxygen-bound form of SHP), reacts rapidly with NO to produce nitrate, whereas SHp(2+)-NO (the No-bound form of SHP) will react with superoxide with the same product formed. it is therefore possible that SHP functions physiologically as a nitric oxide dioxygenase, protecting the organism against NO poisoning, and we propose a possible mechanism for this process.

    Original languageEnglish
    Pages (from-to)992-995
    Number of pages4
    JournalBiochemical Society Transactions
    Volume36
    Issue number5
    DOIs
    Publication statusPublished - Oct 2008
    Event3rd Intracellular Proteolysis Meeting - Canary Isl, Spain
    Duration: 5 Mar 20087 Mar 2008

    Keywords

    • Rhodobacter sphaeroides
    • MECHANISM
    • LIGAND-BINDING
    • c-type cytochrome
    • crystal structure
    • OXYGEN
    • NEUROGLOBIN
    • sphaeroides haem protein
    • nitric oxide dioxygenase
    • dihaem cytochrome c
    • FLAVOHEMOGLOBIN

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  • Cite this

    Li, B-R., Anderson, J. L. R., Mowat, C. G., Miles, C. S., Reid, G. A., & Chapman, S. K. (2008). Rhodobacter sphaeroides haem protein: a novel cytochrome with nitric oxide dioxygenase activity. Biochemical Society Transactions, 36(5), 992-995. https://doi.org/10.1042/BST0360992